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Volumn 41, Issue 2, 2009, Pages 154-162

Biochemical analysis of a papain-like protease isolated from the latex of Asclepias curassavica L.

Author keywords

Asclepiadaceae; Asclepias curassavica; cysteine proteinase; latex; laticifers

Indexed keywords

APOCYNACEAE; ASCLEPIAS; ASCLEPIAS CURASSAVICA;

EID: 64249108291     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmn018     Document Type: Article
Times cited : (42)

References (53)
  • 1
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska M and Zagdañska B. Multifunctional role of plant cysteine proteinases. Acta Bichimica Polonica 2004, 51: 609-624.
    • (2004) Acta Bichimica Polonica , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdañska, B.2
  • 2
  • 3
    • 0002825902 scopus 로고
    • Biochemical mechanisms of disease resistance
    • Bell A. Biochemical mechanisms of disease resistance. Annu Rev Plant Physiol 1981, 32:21-81.
    • (1981) Annu Rev Plant Physiol , vol.32 , pp. 21-81
    • Bell, A.1
  • 4
    • 3042810007 scopus 로고    scopus 로고
    • The plant proteolytic machinery and its role in defence
    • Alvan der Hogrn R and Jones JDG. The plant proteolytic machinery and its role in defence. Curr Opin Plant Biol 2004, 7: 400-407.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 400-407
    • Alvan der Hogrn, R.1    Jones, J.D.G.2
  • 5
    • 0001830556 scopus 로고
    • Roles of proteolytic in interactions of plant with other organisms
    • Dalling MJ ed, Boca Raton: CRC Press
    • Boiler T. Roles of proteolytic in interactions of plant with other organisms. In: Dalling MJ ed. Plant Proteolytic Enzymes. Boca Raton: CRC Press, 1986.
    • (1986) Plant Proteolytic Enzymes
    • Boiler, T.1
  • 6
    • 0037397491 scopus 로고    scopus 로고
    • Functional profiling the proteome with affinity labels
    • Campbell DA and Szardenings AK. Functional profiling the proteome with affinity labels. Curr Opin Chem Biol 2003, 7: 296-303.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 296-303
    • Campbell, D.A.1    Szardenings, A.K.2
  • 7
    • 0000359207 scopus 로고
    • The cysteine proteinases structure and mechanism
    • Journal F and Mc Pherson A. eds, New York: Willey & Sons
    • Baker EN and Drenth J. The cysteine proteinases structure and mechanism. In: Journal F and Mc Pherson A. eds. Biological Macromolecules and Assemblies. New York: Willey & Sons, 1987.
    • (1987) Biological Macromolecules and Assemblies
    • Baker, E.N.1    Drenth, J.2
  • 8
    • 0037376207 scopus 로고    scopus 로고
    • Procerain, a stable cysteine protease from the latex of Calotropis procera
    • Dubey VK and Jagannadham MV. Procerain, a stable cysteine protease from the latex of Calotropis procera. Phytochemistry 2003, 62: 1057-1071.
    • (2003) Phytochemistry , vol.62 , pp. 1057-1071
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 9
    • 0141784573 scopus 로고
    • Proteasas de plantas superiores. Características generales, rol fisiológico y aplica-ciones.
    • Caffini NO, López LMI, Natalucci CL and Priolo NS. Proteasas de plantas superiores. Características generales, rol fisiológico y aplica-ciones. Acta Farm Bonaerense 1988, 7: 195-213.
    • (1988) Acta Farm Bonaerense , vol.7 , pp. 195-213
    • Caffini, N.O.1    López, L.M.I.2    Natalucci, C.L.3    Priolo, N.S.4
  • 10
    • 65249171243 scopus 로고    scopus 로고
    • Raffo L. 2000. http://www.tracker.com.ar/docs/Enzimas.htm.
    • (2000)
    • Raffo, L.1
  • 11
    • 65249140347 scopus 로고    scopus 로고
    • Uhlig H. Industrial Enzymes and their Applications. New York: Willey &Sons 1998, pl-11, 146-179.
    • Uhlig H. Industrial Enzymes and their Applications. New York: Willey &Sons 1998, pl-11, 146-179.
  • 13
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • Vierstra RD. Proteolysis in plants: mechanisms and functions. Plant Mol Biol 1996, 32: 275.
    • (1996) Plant Mol Biol , vol.32 , pp. 275
    • Vierstra, R.D.1
  • 14
    • 0031742430 scopus 로고    scopus 로고
    • Comparison of Asclepiadaceae latex proteases and characterization of Morrenia brachysiephana Griseb. cysteine peptidases
    • Arribere MC, Cortadi A, Gattuso M, Bettiol M, Priolo NS and Caffmi NO. Comparison of Asclepiadaceae latex proteases and characterization of Morrenia brachysiephana Griseb. cysteine peptidases. Phytochem Anal 1998,9: 267-273.
    • (1998) Phytochem Anal , vol.9 , pp. 267-273
    • Arribere, M.C.1    Cortadi, A.2    Gattuso, M.3    Bettiol, M.4    Priolo, N.S.5    Caffmi, N.O.6
  • 15
    • 0034929982 scopus 로고    scopus 로고
    • Comparison of two cysteine endopeptidases from latices of Morrenia brachysiephana Griseb. and Morrenia odorata (Hook et Am.) Lindley (Asclepiadaceae)
    • Vairo Cavalli SE, Cortadi A, Arribere MC, Conforti P, Caffmi NO and Priolo NS. Comparison of two cysteine endopeptidases from latices of Morrenia brachysiephana Griseb. and Morrenia odorata (Hook et Am.) Lindley (Asclepiadaceae). Biol Chem 2001, 382: 879-883.
    • (2001) Biol Chem , vol.382 , pp. 879-883
    • Vairo Cavalli, S.E.1    Cortadi, A.2    Arribere, M.C.3    Conforti, P.4    Caffmi, N.O.5    Priolo, N.S.6
  • 16
    • 0038754124 scopus 로고    scopus 로고
    • Morrenain b I, a papain-like endopeptidase from the latex of Morrenia brachystephana Griseb. (Asclepiadaceae)
    • Vairo Cavalli S, Arribére MC, Cortadi A, Caffini NO and Priolo NS. Morrenain b I, a papain-like endopeptidase from the latex of Morrenia brachystephana Griseb. (Asclepiadaceae). J Protein Chem 2003, 22: 15-22.
    • (2003) J Protein Chem , vol.22 , pp. 15-22
    • Vairo Cavalli, S.1    Arribére, M.C.2    Cortadi, A.3    Caffini, N.O.4    Priolo, N.S.5
  • 20
    • 33748426331 scopus 로고    scopus 로고
    • Hydrolytic profile and isolation of the proteolytic components of latex from Araujia angustifolia frails
    • Obregon WD, Curciarello R, Caffini N and Priolo N. Hydrolytic profile and isolation of the proteolytic components of latex from Araujia angustifolia frails. Acta Farm Bonaerense 2006, 25: 206-212.
    • (2006) Acta Farm Bonaerense , vol.25 , pp. 206-212
    • Obregon, W.D.1    Curciarello, R.2    Caffini, N.3    Priolo, N.4
  • 21
    • 0035170051 scopus 로고    scopus 로고
    • Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae)
    • Trejo SA, López LMI, Cimino CV, Caffini NO and Natalucci CL. Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae). J Protein Chem 2001, 20: 445-453.
    • (2001) J Protein Chem , vol.20 , pp. 445-453
    • Trejo, S.A.1    López, L.M.I.2    Cimino, C.V.3    Caffini, N.O.4    Natalucci, C.L.5
  • 22
    • 16544382613 scopus 로고    scopus 로고
    • Funastrain c II, a cysteine endopeptidase purified from the latex of Funastrum clausum
    • Morcelle del Valle SR, Trejo SA, Canals F, Aviles FX and Priolo NS. Funastrain c II, a cysteine endopeptidase purified from the latex of Funastrum clausum. Protein J 2004, 25: 205-215.
    • (2004) Protein J , vol.25 , pp. 205-215
    • Morcelle del Valle, S.R.1    Trejo, S.A.2    Canals, F.3    Aviles, F.X.4    Priolo, N.S.5
  • 23
    • 65249133810 scopus 로고    scopus 로고
    • Roig JT. Plantas medicinales, aromaticas o venenosas de Cuba-La Habana, Cuba. Ed. Científico-Técnica, Tomo II-2da. ed., 3ra. reimpre-sión. 1945, 426, 428-1125.
    • Roig JT. Plantas medicinales, aromaticas o venenosas de Cuba-La Habana, Cuba. Ed. Científico-Técnica, Tomo II-2da. ed., 3ra. reimpre-sión. 1945, 426, 428-1125.
  • 24
    • 65249099365 scopus 로고    scopus 로고
    • Toursarkissian M. Plantas medicinales de la Argentina. Bs. As., Ed. H. Sur. 1980, 11-178.
    • Toursarkissian M. Plantas medicinales de la Argentina. Bs. As., Ed. H. Sur. 1980, 11-178.
  • 25
    • 16644385670 scopus 로고    scopus 로고
    • Liggieri C, Arribére MC, Trejo SA, Canals F, Avilés F and Priolo N. Purification and biochemical characterization of asclepain c I from the latex Asclepias curassavica L. J Protein 2004, 23: 403-411.
    • Liggieri C, Arribére MC, Trejo SA, Canals F, Avilés F and Priolo N. Purification and biochemical characterization of asclepain c I from the latex Asclepias curassavica L. J Protein 2004, 23: 403-411.
  • 26
    • 65249170431 scopus 로고
    • Argentina de Agricultura y Jardinería
    • Buenos Aires
    • Dimitri M. Enciclopedia Argentina de Agricultura y Jardinería. Acme SACI, Buenos Aires 1972, 774-780.
    • (1972) Acme SACI , pp. 774-780
    • Enciclopedia, D.M.1
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein dye binding. Anal Biochem 1976, 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0015477165 scopus 로고
    • Hydrogen ion buffers
    • Good NE and Izawa S. Hydrogen ion buffers. Meth Enzymol 1972, 24: 53-68.
    • (1972) Meth Enzymol , vol.24 , pp. 53-68
    • Good, N.E.1    Izawa, S.2
  • 30
    • 65249088309 scopus 로고    scopus 로고
    • Dunn BM. In: Beynon R and Bond JS eds. Determination of Protease Mechanism. Proteolytic Enzymes, a Practical Approach. Oxford: IRL Press, 2001.
    • Dunn BM. In: Beynon R and Bond JS eds. Determination of Protease Mechanism. Proteolytic Enzymes, a Practical Approach. Oxford: IRL Press, 2001.
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Shägger H and Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987, 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Shägger, H.1    Von Jagow, G.2
  • 34
    • 0016334079 scopus 로고
    • The assay of the bromelains using N-CBZ-L-lysiue p-nitrophenyl ester and N-CBZ-L-glicine p-nitrophenyl ester as substrates
    • Silverstein RM. The assay of the bromelains using N-CBZ-L-lysiue p-nitrophenyl ester and N-CBZ-L-glicine p-nitrophenyl ester as substrates. Anal Biochem 1974, 62: 478-484.
    • (1974) Anal Biochem , vol.62 , pp. 478-484
    • Silverstein, R.M.1
  • 35
    • 0021672206 scopus 로고
    • L-pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide - a chromogenic substrate for thiol proteinase assay
    • Filippova IYu, Lysogorskaya EN, Oksenoit ES, Rudenskaya GN and Stepanov VM. L-pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide - a chromogenic substrate for thiol proteinase assay. Anal Biochem 1984, 143: 293-297.
    • (1984) Anal Biochem , vol.143 , pp. 293-297
    • IYu, F.1    Lysogorskaya, E.N.2    Oksenoit, E.S.3    Rudenskaya, G.N.4    Stepanov, V.M.5
  • 39
    • 0019324038 scopus 로고
    • Multiple forms of the asclepains, cysteinyl proteases from milkweed
    • Lynn KR, Brockbank WJ and Clevette NA. Multiple forms of the asclepains, cysteinyl proteases from milkweed. Biochim Biophys Acta 1980,612: 119-125.
    • (1980) Biochim Biophys Acta , vol.612 , pp. 119-125
    • Lynn, K.R.1    Brockbank, W.J.2    Clevette, N.A.3
  • 40
    • 0018799155 scopus 로고
    • Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed)
    • Brockbank WJ and Lynn KR. Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed). Biochim Biophys Acta 1979, 578: 113-122.
    • (1979) Biochim Biophys Acta , vol.578 , pp. 113-122
    • Brockbank, W.J.1    Lynn, K.R.2
  • 42
    • 33746784661 scopus 로고    scopus 로고
    • Isolation and characterization of hieronymain II, another peptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae)
    • Bruno M, Trejo S, Avilés X, Caffini NO and López L. Isolation and characterization of hieronymain II, another peptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae). Protein J 2006, 25: 224-231.
    • (2006) Protein J , vol.25 , pp. 224-231
    • Bruno, M.1    Trejo, S.2    Avilés, X.3    Caffini, N.O.4    López, L.5
  • 43
    • 45849146597 scopus 로고    scopus 로고
    • Occurrence and properties of proteases in plant lattices
    • Domsalla A and Melzig MF. Occurrence and properties of proteases in plant lattices. Planta Med 2008, 74: 699-711.
    • (2008) Planta Med , vol.74 , pp. 699-711
    • Domsalla, A.1    Melzig, M.F.2
  • 44
    • 51249107963 scopus 로고    scopus 로고
    • Plant cysteine proteinases: Evaluation of the pharmacological activity
    • Salas CE, Gomes MTR, Hernandez M and Lopes MTP. Plant cysteine proteinases: evaluation of the pharmacological activity. Phytochemistry 2008, 69: 2263-2269.
    • (2008) Phytochemistry , vol.69 , pp. 2263-2269
    • Salas, C.E.1    Gomes, M.T.R.2    Hernandez, M.3    Lopes, M.T.P.4
  • 45
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-mduced expression of multiple cysteine proteinases of rice seeds (oryzains)
    • Watanabe H, Abe K, Emori Y, Hosoyama H and Arai SJ. Molecular cloning and gibberellin-mduced expression of multiple cysteine proteinases of rice seeds (oryzains). Biol Chem 1991, 266: 16897-16902.
    • (1991) Biol Chem , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.J.5
  • 46
    • 0030108838 scopus 로고    scopus 로고
    • Induction of cysteine and serine proteases during phylogenesis in Zinnia elegans
    • Ye ZH and Varner JE. Induction of cysteine and serine proteases during phylogenesis in Zinnia elegans. Plant Mol Biol 1996, 30: 1233 1246.
    • (1996) Plant Mol Biol , vol.30 , pp. 1233-1246
    • Ye, Z.H.1    Varner, J.E.2
  • 47
    • 0027269410 scopus 로고
    • Nucleotide sequence and expression in Escherichia coli of cDNAs encoding papaya proteinase omega from Carica papaya
    • Revell DF, Cummings NJ, Baker KC, Collins ME, Taylor MA, Sumner IG and Pickersgill RW, et al. Nucleotide sequence and expression in Escherichia coli of cDNAs encoding papaya proteinase omega from Carica papaya. Gene 1993, 127: 221-225.
    • (1993) Gene , vol.127 , pp. 221-225
    • Revell, D.F.1    Cummings, N.J.2    Baker, K.C.3    Collins, M.E.4    Taylor, M.A.5    Sumner, I.G.6    Pickersgill, R.W.7
  • 48
    • 0022828086 scopus 로고
    • Cloning and sequencing of papain-encoding cDNA
    • Cohen LW, Coghlan VM and Dihel LC. Cloning and sequencing of papain-encoding cDNA. Gene 1986, 48: 219-227.
    • (1986) Gene , vol.48 , pp. 219-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihel, L.C.3
  • 49
    • 0032585341 scopus 로고    scopus 로고
    • Asamizu E, Sato S, Kaneko T, Nakamura Y, Kotani H, Miyajima N and Tabata S. Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned Pl and TAC clones. DNA Res 1998, 5: 379-391.
    • Asamizu E, Sato S, Kaneko T, Nakamura Y, Kotani H, Miyajima N and Tabata S. Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned Pl and TAC clones. DNA Res 1998, 5: 379-391.
  • 50
    • 0037336595 scopus 로고    scopus 로고
    • Identification of dehydration-responsive cysteine proteases during post-harvest senescence of broccoli florets
    • Coupe SA, Sinclair BK, Watson LM, Heyes JA and Eason JR. Identification of dehydration-responsive cysteine proteases during post-harvest senescence of broccoli florets. J Exp Bot 2003, 54: 1045-1056.
    • (2003) J Exp Bot , vol.54 , pp. 1045-1056
    • Coupe, S.A.1    Sinclair, B.K.2    Watson, L.M.3    Heyes, J.A.4    Eason, J.R.5
  • 51
    • 0029098094 scopus 로고
    • Isolation and characterization of two distinct cDNA clones encoding com seed cysteine proteinases
    • Domoto C, Watanate H, Abe K and Arai S. Isolation and characterization of two distinct cDNA clones encoding com seed cysteine proteinases. Biochem Biophysis Acta 1995, 1263: 241-244.
    • (1995) Biochem Biophysis Acta , vol.1263 , pp. 241-244
    • Domoto, C.1    Watanate, H.2    Abe, K.3    Arai, S.4
  • 53
    • 0034890897 scopus 로고    scopus 로고
    • Isolation and characterization of a gene encoding a drought-induced cysteine protease in tomato (Lycopersicon esculentum)
    • Harrak H, Azelmat S, Baker EN and Tabaeizadeh Z. Isolation and characterization of a gene encoding a drought-induced cysteine protease in tomato (Lycopersicon esculentum). Genome 2001, 44: 368-374.
    • (2001) Genome , vol.44 , pp. 368-374
    • Harrak, H.1    Azelmat, S.2    Baker, E.N.3    Tabaeizadeh, Z.4


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